protein kinase C binding

Definition

Target type: molecularfunction

Binding to protein kinase C. [GOC:jl]

Protein kinase C (PKC) binding is a molecular function that involves the interaction of proteins with the catalytic domain of PKC enzymes. PKC is a family of serine/threonine-specific protein kinases that play a crucial role in signal transduction pathways. They are activated by various stimuli, including diacylglycerol (DAG), calcium ions (Ca2+), and phosphatidylserine (PS), and their activation leads to phosphorylation of target proteins, thereby regulating a wide range of cellular processes.

PKC binding proteins typically contain a specific motif known as a PKC consensus sequence, which is characterized by a cluster of basic amino acids (arginine and lysine) followed by a hydrophobic residue. This motif interacts with the catalytic domain of PKC, enabling the enzyme to phosphorylate the target protein.

The molecular function of PKC binding can be broadly classified into two categories:

1. **Activation of PKC:** Some proteins bind to PKC to enhance its activity. These proteins can act as cofactors, promoting the translocation of PKC to the plasma membrane or facilitating its interaction with substrates.

2. **Regulation of PKC signaling:** Other proteins bind to PKC to modulate its activity or regulate its downstream signaling pathways. These proteins can act as inhibitors, suppressing PKC activity, or as scaffolding proteins, organizing PKC and other signaling molecules into functional complexes.

The specific function of PKC binding depends on the context and the identity of the interacting proteins.

Overall, PKC binding is a crucial molecular function that plays a central role in regulating a wide range of cellular processes, including cell growth, differentiation, apoptosis, and inflammation.'
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Proteins (24)

Compounds (1,200)